5kzd: Difference between revisions
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==N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol== | |||
<StructureSection load='5kzd' size='340' side='right' caption='[[5kzd]], [[Resolution|resolution]] 2.33Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5kzd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KZD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RCJ:(2~{S},4~{S},5~{R},6~{R},7~{S},8~{R})-5-ACETAMIDO-2,4,6,7,8,9-HEXAKIS(OXIDANYL)NONANOIC+ACID'>RCJ</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kze|5kze]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kzd OCA], [http://pdbe.org/5kzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kzd RCSB], [http://www.ebi.ac.uk/pdbsum/5kzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kzd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NANA_STAA3 NANA_STAA3]] Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. In this study, we analyzed the kinetic parameters of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus (MRSA). We determined that the enzyme has a relatively high KM of 3.2 mm, suggesting that flux through the catabolic pathway is likely to be controlled by this enzyme. Our data indicate that sialic acid alditol, a known inhibitor of N-acetylneuraminate lyase enzymes, is a stronger inhibitor of MRSA N-acetylneuraminate lyase than of Clostridium perfringens N-acetylneuraminate lyase. Our analysis of the crystal structure of ligand-free and 2R-sialic acid alditol-bound MRSA N-acetylneuraminate lyase suggests that subtle dynamic differences in solution and/or altered binding interactions within the active site may account for species-specific inhibition. | |||
Structure and inhibition of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus.,North RA, Watson AJ, Pearce FG, Muscroft-Taylor AC, Friemann R, Fairbanks AJ, Dobson RC FEBS Lett. 2016 Dec;590(23):4414-4428. doi: 10.1002/1873-3468.12462. Epub 2016, Nov 7. PMID:27943302<ref>PMID:27943302</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5kzd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: N-acetylneuraminate lyase]] | |||
[[Category: Dobson, R C.J]] | |||
[[Category: Fairbanks, A J]] | |||
[[Category: Friemann, R]] | |||
[[Category: Muscroft-Taylor, A C]] | |||
[[Category: North, R A]] | |||
[[Category: Pearce, F G]] | |||
[[Category: Watson, A J.A]] | |||
[[Category: Inhibitor]] | |||
[[Category: Lyase]] | |||
[[Category: Tim-barrel]] | |||
Revision as of 16:30, 18 January 2017
N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol
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